A single common portal for clathrin-mediated endocytosis of distinct cargo governed by cargo-selective adaptors

Peter Keyel, Sanjay K Mishra, Robyn Roth, John E Heuser, Simon C Watkins, Linton M Traub

Research output: Contribution to journalArticle

Abstract

Sorting of transmembrane cargo into clathrin-coated vesicles requires endocytic adaptors, yet RNA interference (RNAi)-mediated gene silencing of the AP-2 adaptor complex only disrupts internalization of a subset of clathrin-dependent cargo. This suggests alternate clathrin-associated sorting proteins participate in cargo capture at the cell surface, and a provocative recent proposal is that discrete endocytic cargo are sorted into compositionally and functionally distinct clathrin coats. We show here that the FXNPXY-type internalization signal within cytosolic domain of the LDL receptor is recognized redundantly by two phosphotyrosine-binding domain proteins, Dab2 and ARH; diminishing both proteins by RNAi leads to conspicuous LDL receptor accumulation at the cell surface. AP-2-dependent uptake of transferrin ensues relatively normally in the absence of Dab2 and ARH, clearly revealing delegation of sorting operations at the bud site. AP-2, Dab2, ARH, transferrin, and LDL receptors are
Original languageEnglish
Pages (from-to)4300-4317
JournalMolecular Biology of the Cell
StatePublished - 2006

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